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The tubulin code: Molecular components, readout mechanisms, and functions

Microtubules are cytoskeletal filaments that are dynamically assembled from α/β-tubulin heterodimers. The primary sequence and structure of the tubulin proteins and, consequently, the properties and architecture of microtubules are highly conserved in eukaryotes. Despite this conservation, tubulin i...

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Detalles Bibliográficos
Autor principal: Janke, Carsten
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4137062/
https://www.ncbi.nlm.nih.gov/pubmed/25135932
http://dx.doi.org/10.1083/jcb.201406055
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author Janke, Carsten
author_facet Janke, Carsten
author_sort Janke, Carsten
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description Microtubules are cytoskeletal filaments that are dynamically assembled from α/β-tubulin heterodimers. The primary sequence and structure of the tubulin proteins and, consequently, the properties and architecture of microtubules are highly conserved in eukaryotes. Despite this conservation, tubulin is subject to heterogeneity that is generated in two ways: by the expression of different tubulin isotypes and by posttranslational modifications (PTMs). Identifying the mechanisms that generate and control tubulin heterogeneity and how this heterogeneity affects microtubule function are long-standing goals in the field. Recent work on tubulin PTMs has shed light on how these modifications could contribute to a “tubulin code” that coordinates the complex functions of microtubules in cells.
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spelling pubmed-41370622015-02-18 The tubulin code: Molecular components, readout mechanisms, and functions Janke, Carsten J Cell Biol Reviews Microtubules are cytoskeletal filaments that are dynamically assembled from α/β-tubulin heterodimers. The primary sequence and structure of the tubulin proteins and, consequently, the properties and architecture of microtubules are highly conserved in eukaryotes. Despite this conservation, tubulin is subject to heterogeneity that is generated in two ways: by the expression of different tubulin isotypes and by posttranslational modifications (PTMs). Identifying the mechanisms that generate and control tubulin heterogeneity and how this heterogeneity affects microtubule function are long-standing goals in the field. Recent work on tubulin PTMs has shed light on how these modifications could contribute to a “tubulin code” that coordinates the complex functions of microtubules in cells. The Rockefeller University Press 2014-08-18 /pmc/articles/PMC4137062/ /pubmed/25135932 http://dx.doi.org/10.1083/jcb.201406055 Text en © 2014 Janke This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Reviews
Janke, Carsten
The tubulin code: Molecular components, readout mechanisms, and functions
title The tubulin code: Molecular components, readout mechanisms, and functions
title_full The tubulin code: Molecular components, readout mechanisms, and functions
title_fullStr The tubulin code: Molecular components, readout mechanisms, and functions
title_full_unstemmed The tubulin code: Molecular components, readout mechanisms, and functions
title_short The tubulin code: Molecular components, readout mechanisms, and functions
title_sort tubulin code: molecular components, readout mechanisms, and functions
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4137062/
https://www.ncbi.nlm.nih.gov/pubmed/25135932
http://dx.doi.org/10.1083/jcb.201406055
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